Structure of PDB 3kp0 Chain B

Receptor sequence
>3kp0B (length=728) Species: 1511 (Acetoanaerobium sticklandii) [Search protein sequence]
LQLRVNEKLDVENILKDLDKYTPKRRGWTWRQPAENLQMGPFIYKDASTP
LENSVALPSAKYFGDIDPQPLPVITTEIASGRFEDDIRRMRMAAWHGADH
IMVIRTAGQSHYDGLIEGTPQGIGGVPITRKQVRAQRKALDLIEEEVGRP
INYHSYVSGVAGPDIAVMFAEEGVNGAHQDPQYNVLYRNINMIRSFIDAC
ESKTIMAWADMAQIDGAHNANATAREAWKVMPELMVQHALNSIFSLKVGM
KKSNICLSTVPPTAPPAPSMYLDLPYAVALREMFEGYRMRAQMNTKYMEA
STREATVTHVLNLLISKLTRADIQSTITPDEGRNVPWHIYNIEACDTAKQ
ALIGMDGLMDMVQLKREGVLGDTVRELKERAVLFMEEIIEAGGYFNAVEQ
GFFVDSGYYPERNGDGIARQINGGIGAGTVFERDEDYMAPVTAHFGYNNV
KQYDEALVSEPSKLIDGCTLEVPEKIVYIDELDENDNVNVRMEETKEFRS
MIKPEVEWQADGTVLLTMFLPTSKRVAEFAAIEFAKKMNLEEVEVINREV
MQEAEGTRIELKGRVPFSIDINSLVIPPILSEDEIREDIEKTPLKIVAAT
VGEDEHSVGLREVIDIKHGGIEKYGVEVHYLGTSVPVEKLVDAAIELKAD
AILASTIISHDDIHYKNMKRIHELAVEKGIRDKIMIGCGGTQVTPEVAVK
QGVDAGFGRGSKGIHVATFLVKKRREMR
3D structure
PDB3kp0 Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase.
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y187 H225 R297 K629
Catalytic site (residue number reindexed from 1) Y183 H218 R290 K617
Enzyme Commision number 5.4.3.5: D-ornithine 4,5-aminomutase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
GO:0046983 protein dimerization activity
GO:0047831 D-ornithine 4,5-aminomutase activity

View graph for
Molecular Function
External links
PDB RCSB:3kp0, PDBe:3kp0, PDBj:3kp0
PDBsum3kp0
PubMed20106986
UniProtE3PY95|OAME_ACESD D-ornithine 4,5-aminomutase subunit beta (Gene Name=oraE)

[Back to BioLiP]